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Prospects for treatment of free radical-mediated tissu injury

doi:10.1016/S0092-8674(01)00383-X

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Holland W.L., Adams A.C., Brozinick J.T., et al

Ferreira et al., 2016)

This increase in activity appears to result from a decrease in the Km GSH and a large increase in the catalytic efficiency of the enzyme I10A/G112C - mutant displays significant decrease in 1-chloro-2,4-dinitrobenzene activity I10C - mutant displays significant decrease in 1-chloro-2,4-dinitrobenzene activity I44A - site-directed mutagenesis, H-site mutation, the mutant shows reduced activity compared to the wild-type enzyme I71V site-directed mutagensis, structure analysis II71A site-directed mutagensis, structure analysis K196N O43708, Q9H4Y5, Q16772, P09211, P09210, P08263, P09488, O15217, P28161, Q03013, P46439, P78417, O60760, Q7RTV2, P21266, P0CG30 naturally occuring polymorphism K62A - site-directed mutagenesis, G-site mutation, the mutant shows reduced activity compared to the wild-type enzyme K62E - site-directed mutagenesis, G-site mutation, the mutant shows reduced activity compared to the wild-type enzyme L158I O43708, Q9H4Y5, Q16772, P09211, P09210, P08263, P09488, O15217, P28161, Q03013, P46439, P78417, O60760, Q7RTV2, P21266, P0CG30 naturally occuring mutation, the substitution is rare and may generate unstable protein L15A - site-directed mutagenesis, H-site mutation, the mutant shows reduced activity compared to the wild-type enzyme L183A - site-directed mutagenesis, G-site mutation, the mutant shows reduced activity compared to the wild-type enzyme L58A - site-directed mutagenesis, H-site mutation, the mutant shows reduced activity compared to the wild-type enzyme L88A - site-directed mutagenesis, H-site mutation, the mutant shows reduced activity compared to the wild-type enzyme L92A - site-directed mutagenesis, H-site mutation, inactive mutant M212C - site-directed mutagensis of isozyme GST M2-2, mutation of the catalytic site residue M212